Evidence map›Paper›PMID 24786756›Full record

ReviewBiochemistry2014

Mammalian O-mannosylation pathway: glycan structures, enzymes, and protein substrates.

Jeremy L Praissman, Lance Wells

Abstract readReview
In one paragraph

Review in Biochemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

37 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Review
  7. Review
  8. Article
  9. Article
  10. Review
  11. Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Facile Chemoenzymatic Synthesis of O-Mannosyl Glycans.Angewandte Chemie (International ed. in English) · 2018
    Article
  18. Chemoenzymatic Assembly of Mammalian O-Mannose Glycans.Angewandte Chemie (International ed. in English) · 2018
    Article
  19. Novel Myopia Genes and Pathways Identified From Syndromic Forms of Myopia.Investigative ophthalmology & visual science · 2018
    Article
  20. Discovery of an O-mannosylation pathway selectively serving cadherins and protocadherins.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

2 authors.

Jeremy L PraissmanComplex Carbohydrate Research Center, Department of Biochemistry and Molecular Biology, The University of Georgia , Athens, Georgia 30602, United States.
Lance Wells

Funding

TR&D1: Stem Cell and Induced Pluripotent Stem Cell Resources (Pages 116-134)P41GM103490 · NIGMS · UNIVERSITY OF GEORGIA · PI PIERCE, J. MICHAEL · 2012 to 2018
$13.7M
Recombinant Production of Glycosylation Enzymes for Biochem/Structural StudiesP01GM107012 · NIGMS · UNIVERSITY OF GEORGIA · PI PRESTEGARD, JAMES H. · 2013 to 2017
$7.5M
NIGMS NIH HHS P01GM107012NIGMS NIH HHS P41 GM103490NIGMS NIH HHS P41GM103490
6 · The paper itself

Abstract

The mammalian O-mannosylation pathway for protein post-translational modification is intricately involved in modulating cell-matrix interactions in the musculature and nervous system. Defects in enzymes of this biosynthetic pathway are causative for multiple forms of congenital muscular dystophy. The application of advanced genetic and biochemical technologies has resulted in remarkable progress in this field over the past few years, culminating with the publication of three landmark papers in 2013 alone. In this review, we will highlight recent progress focusing on the dramatic expansion of the set of genes known to be involved in O-mannosylation and disease processes, the concurrent acceleration of the rate of O-mannosylation pathway protein functional assignments, the tremendous increase in the number of proteins now known to be modified by O-mannosylation, and the recent progress in protein O-mannose glycan quantification and site assignment. Also, we attempt to highlight key outstanding questions raised by this abundance of new information.

Indexed as

AnimalsCarbohydrate ConformationGlycosylationHumansMannoseMannosyltransferasesPolysaccharidesProtein Processing, Post-TranslationalMannoseMannosyltransferasesPolysaccharides

Identifiers

PMID24786756
PMCPMC4033628

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.